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Conserved domains on  [gi|460411713|ref|XP_004251250|]
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probable calcium-binding protein CML13 [Solanum lycopersicum]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 1-147 3.74e-46

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 147.22  E-value: 3.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   1 MGKDLSNDQISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAEEKL--TSPFDFNRFMELMSKHLKPE 78
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgNGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460411713  79 PFDRQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARMVAK 147
Cdd:PTZ00184  81 DSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-147 3.74e-46

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 147.22  E-value: 3.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   1 MGKDLSNDQISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAEEKL--TSPFDFNRFMELMSKHLKPE 78
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgNGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460411713  79 PFDRQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARMVAK 147
Cdd:PTZ00184  81 DSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
9-144 4.83e-13

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   9 QISSMKEAFTLFDTDGDGKISPSELGILMRslgGNPTQAQLKSIIAEEKLTSPFDFNRFMElmskHLKPEPFDRQLRDAF 88
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFR---RLWATLFSEADTDGDGRISREEFVAGME----SLFEATVEPFARAAF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713  89 KVLDKDGTGFVVVSDLKHILTSIGekLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 83-144 3.80e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 57.56  E-value: 3.80e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460411713  83 QLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
81-144 1.47e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 1.47e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713   81 DRQLRDAFKVLDKDGTGFVVVSDLKHILTSI--GEKLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 13-40 1.56e-05

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 39.67  E-value: 1.56e-05
                           10        20
                   ....*....|....*....|....*...
gi 460411713    13 MKEAFTLFDTDGDGKISPSELGILMRSL 40
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
14-144 7.91e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 35.04  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  14 KEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAeeKLTSPFDFNRFMELMSKHLKPEPFDR------QLRDA 87
Cdd:NF041410  30 KQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFS--DLDSDGDGSLSSDELAAAAPPPPPPPdqapstELADD 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 460411713  88 -FKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFdewIREVDAGSDGKIRYEDFIARM 144
Cdd:NF041410 108 lLSALDTDGDGSISSDELSAGLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAAL 162
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1-147 3.74e-46

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 147.22  E-value: 3.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   1 MGKDLSNDQISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAEEKL--TSPFDFNRFMELMSKHLKPE 78
Cdd:PTZ00184   1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgNGTIDFPEFLTLMARKMKDT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460411713  79 PFDRQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARMVAK 147
Cdd:PTZ00184  81 DSEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
PTZ00183 PTZ00183
centrin; Provisional
 4-144 1.51e-27

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 100.15  E-value: 1.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   4 DLSNDQISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAEEK--LTSPFDFNRFMELMSKHLKPEPFD 81
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDkdGSGKIDFEEFLDIMTKKLGERDPR 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460411713  82 RQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:PTZ00183  90 EEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
9-144 4.83e-13

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   9 QISSMKEAFTLFDTDGDGKISPSELGILMRslgGNPTQAQLKSIIAEEKLTSPFDFNRFMElmskHLKPEPFDRQLRDAF 88
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFR---RLWATLFSEADTDGDGRISREEFVAGME----SLFEATVEPFARAAF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713  89 KVLDKDGTGFVVVSDLKHILTSIGekLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:COG5126   76 DLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 83-144 3.80e-12

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 57.56  E-value: 3.80e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460411713  83 QLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 54-140 1.41e-11

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 57.54  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  54 AEEKLTSPFDFNRFMELMSKHLKPEPFDRQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEK-----LEPSEFDEWIREVD 128
Cdd:cd16252    9 SEMRHHGSFNYSKFFEYMQKFQTSEQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAAD 88

                         90
                 ....*....|..
gi 460411713 129 AGSDGKIRYEDF 140
Cdd:cd16252   89 TDGDGRIDFQEF 100
EF-hand_7 pfam13499
EF-hand domain pair;
81-144 1.47e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 1.47e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713   81 DRQLRDAFKVLDKDGTGFVVVSDLKHILTSI--GEKLEPSEFDEWIREVDAGSDGKIRYEDFIARM 144
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 14-55 4.68e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 49.47  E-value: 4.68e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 460411713  14 KEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAE 55
Cdd:cd00051    3 REAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIRE 44
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 49-146 1.33e-08

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 49.45  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  49 LKSIIAEEKLTSPFDFNRFMELMSKHLKPEPfdrQLRDAFKVLDKDGTGFVVVSDLKHIL---TSIGEKLEPSEFDEWIR 125
Cdd:cd16251    4 IEKAPSAFRAHGSFNYKKFFEHVGLKQKSED---QIKKVFQILDKDKSGFIEEEELKYILkgfSIAGRDLTDEETKALLA 80

                         90       100
                 ....*....|....*....|.
gi 460411713 126 EVDAGSDGKIRYEDFiARMVA 146
Cdd:cd16251   81 AGDTDGDGKIGVEEF-ATLVA 100
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 13-75 4.01e-08

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 47.34  E-value: 4.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460411713  13 MKEAFTLFDTDGDGKISPSELGILMRSLGGNPTqaqlksiiAEEKLTSP--FDFNRFMELMSKHL 75
Cdd:cd22949    5 FREAFILFDRDGDGELTMYEAVLAMRSCGIPLT--------NDEKDALPasMNWDQFENWAKKKL 61
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 10-102 8.49e-07

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 45.98  E-value: 8.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  10 ISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIiaeekltspfdFNRFMELMSKHLKpepFDR------- 82
Cdd:cd16180   66 IQDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLL-----------VRKFDRRRRGSIS---FDDfveacvt 131

                         90       100
                 ....*....|....*....|..
gi 460411713  83 --QLRDAFKVLDKDGTGFVVVS 102
Cdd:cd16180  132 lkRLTDAFRKYDTNRTGYATIS 153
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 12-141 7.40e-06

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 43.29  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  12 SMKEAFTLFDTDGDGKISPSELGILMRSlgGNPTQAQLKSIiaeEKLTSPFDFNRfmelmSKHLKPEPFDR------QLR 85
Cdd:cd16180    1 ELRRIFQAVDRDRSGRISAKELQRALSN--GDWTPFSIETV---RLMINMFDRDR-----SGTINFDEFVGlwkyiqDWR 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713  86 DAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFI 141
Cdd:cd16180   71 RLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFV 126
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 13-40 1.56e-05

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 39.67  E-value: 1.56e-05
                           10        20
                   ....*....|....*....|....*...
gi 460411713    13 MKEAFTLFDTDGDGKISPSELGILMRSL 40
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_6 pfam13405
EF-hand domain;
13-41 1.68e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.47  E-value: 1.68e-05
                          10        20
                  ....*....|....*....|....*....
gi 460411713   13 MKEAFTLFDTDGDGKISPSELGILMRSLG 41
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 25-142 1.73e-05

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 42.36  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  25 DGKISPSELG-ILMRS-LGGNPTQAQLKS---IIA--EEKLTSPFDFNRFMELMSKHlkpepfdRQLRDAFKVLDKDGTG 97
Cdd:cd16181   13 DGQIDADELQrCLTQSgISGNYQPFSLETcrlMIAmlDRDHSGKMGFNEFKELWAAL-------NQWKTTFMQYDRDRSG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 460411713  98 FVVVSDLKHILTSIGEKLEPSEFDEWIREVdaGSDGKIRYEDFIA 142
Cdd:cd16181   86 TVEPQELQQAIRSFGYNLSPQALNVIVKRY--SKNGRITFDDFVA 128
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 82-145 5.59e-05

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 41.03  E-value: 5.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460411713  82 RQLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWI-REVDAgsDGKIRYEDFIARMV 145
Cdd:cd16196   71 RSWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNATLNALVlRYSNK--DGRISFDDFIMCAV 133
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 3-102 1.18e-04

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.11  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713   3 KDLSNdQISSMKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAE-EKLTSPFDFNRFMELMSkhlkpepFD 81
Cdd:cd15897   63 KGLWN-YIKAWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRyDRGRGNIDFDDFIQCCV-------RL 134

                         90       100
                 ....*....|....*....|.
gi 460411713  82 RQLRDAFKVLDKDGTGFVVVS 102
Cdd:cd15897  135 QRLTDAFRRYDKDQDGQIQVN 155
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 47-147 1.26e-04

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 39.04  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  47 AQLKSIIAEEKLTSPFDFNRFMELMSkhLKPEPFDrQLRDAFKVLDKDGTGFVVVSDLKHIL---TSIGEKLEPSEFDEW 123
Cdd:cd16254    2 EDIKKAVGAFAAADSFDYKKFFEMVG--LKKKSAD-DVKKVFHILDKDKSGFIEEDELKFVLkgfSPDGRDLSDKETKAL 78

                         90       100
                 ....*....|....*....|....
gi 460411713 124 IREVDAGSDGKIRYEDFIArMVAK 147
Cdd:cd16254   79 LAAGDKDGDGKIGIDEFAT-LVAE 101
PTZ00183 PTZ00183
centrin; Provisional
 83-147 1.34e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.67  E-value: 1.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460411713  83 QLRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIARMVAK 147
Cdd:PTZ00183  18 EIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKK 82
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 13-40 1.67e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.99  E-value: 1.67e-04
                          10        20
                  ....*....|....*....|....*...
gi 460411713   13 MKEAFTLFDTDGDGKISPSELGILMRSL 40
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_6 pfam13405
EF-hand domain;
83-112 2.20e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.39  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 460411713   83 QLRDAFKVLDKDGTGFVVVSDLKHILTSIG 112
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 85-141 2.89e-04

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 38.77  E-value: 2.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 460411713  85 RDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFI 141
Cdd:cd16183   70 QNCFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFDDFI 126
EF-hand_7 pfam13499
EF-hand domain pair;
10-55 4.76e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.46  E-value: 4.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 460411713   10 ISSMKEAFTLFDTDGDGKISPSELGILMRSL--GGNPTQAQLKSIIAE 55
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKE 48
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 12-142 5.17e-04

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 38.18  E-value: 5.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  12 SMKEAFTLFDTDgDGKISPSELGILMRSLGGNPTQAQLkSIIAEEKLTSPFD--------FNRFMELMSKHLKpepfdrq 83
Cdd:cd15897    1 QLRNVFQAVAGD-DGEISATELQQALSNVGWTHFDLGF-SLETCRSMIAMMDrdhsgklnFSEFKGLWNYIKA------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 460411713  84 LRDAFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSdGKIRYEDFIA 142
Cdd:cd15897   72 WQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDRGR-GNIDFDDFIQ 129
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 13-142 1.39e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 36.81  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  13 MKEAFTLFDTDGDGKISPSEL-GILmrSLGGnptqaQLKSIIAEEKLTSPFDFNR-----FMELMSKHlkpePFDRQLRD 86
Cdd:cd16185    2 LRQWFRAVDRDRSGSIDVNELqKAL--AGGG-----LLFSLATAEKLIRMFDRDGngtidFEEFAALH----QFLSNMQN 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713  87 AFKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFIA 142
Cdd:cd16185   71 GFEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIE 126
EF-hand_5 pfam13202
EF hand;
13-37 1.80e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.83  E-value: 1.80e-03
                          10        20
                  ....*....|....*....|....*
gi 460411713   13 MKEAFTLFDTDGDGKISPSELGILM 37
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 23-145 1.86e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 36.43  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  23 DGDGKISPSELGILMRSL----GGNPTQAQL---KSIIA--EEKLTSPFDFNRFMELMSKhLKpepfdrQLRDAFKVLDK 93
Cdd:cd16182   11 GEDEEIDAVELQKLLNASllkdMPKFDGFSLetcRSLIAlmDTNGSGRLDLEEFKTLWSD-LK------KWQAIFKKFDT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 460411713  94 DGTGFVVVSDLKHILTSIGEKLePSEFDEWIREVDAGSDGKIRYEDFIARMV 145
Cdd:cd16182   84 DRSGTLSSYELRKALESAGFHL-SNKVLQALVLRYADSTGRITFEDFVSCLV 134
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 13-144 3.46e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 35.34  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  13 MKEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAE-EKLTSPF-DFNRFMELMSKHL-KPEpfdrqLRDAFK 89
Cdd:cd15898    2 LRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEvDTNGDGTlTFDEFEELYKSLTeRPE-----LEPIFK 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 460411713  90 VLDKDGTGFVVVSDLKHILTSI-GEKLEPSEFDEWIREVD-AGSDGKIRYEDFIARM 144
Cdd:cd15898   77 KYAGTNRDYMTLEEFIRFLREEqGENVSEEECEELIEKYEpERENRQLSFEGFTNFL 133
EFh_parvalbumin_beta cd16255
EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed ...
 83-145 6.26e-03

EF-hand, calcium binding motif, found in beta-parvalbumin; Beta-parvalbumin, also termed Oncomodulin-1 (OM), is a small calcium-binding protein that is expressed in hepatomas, as well as in the blastocyst and the cytotrophoblasts of the placenta. It is also found to be expressed in the cochlear outer hair cells of the organ of Corti and frequently expressed in neoplasms. Mammalian beta-parvalbumin is secreted by activated macrophages and neutrophils. It may function as a tissue-specific Ca2+-dependent regulatory protein, and may also serve as a specialized cytosolic Ca2+ buffer. Beta-parvalbumin acts as a potent growth-promoting signal between the innate immune system and neurons in vivo. It has high and specific affinity for its receptor on retinal ganglion cells (RGC) and functions as the principal mediator of optic nerve regeneration. It exerts its effects in a cyclic adenosine monophosphate (cAMP)-dependent manner and can further elevate intracellular cAMP levels. Moreover, beta-parvalbumin is associated with efferent function and outer hair cell electromotility, and can identify different hair cell types in the mammalian inner ear. Beta-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. The EF site displays a high-affinity for Ca2+/Mg2+, and the CD site is a low-affinity Ca2+-specific site. In addition, beta-parvalbumin is distinguished from other parvalbumins by its unusually low isoelectric point (pI = 3.1) and sequence eccentricities (e.g., Y57-L58-D59 instead of F57-I58-E59).


Pssm-ID: 319998 [Multi-domain]  Cd Length: 101  Bit Score: 34.32  E-value: 6.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460411713  83 QLRDAFKVLDKDGTGFVVVSDLKHIL---TSIGEKLEPSEFDEWIREVDAGSDGKIRYEDFiARMV 145
Cdd:cd16255   35 DVKKVFEIIDQDKSGFIEEEELKLFLqnfSSGARELTDAETKAFLKAGDSDGDGKIGVEEF-QALV 99
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
14-144 7.91e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 35.04  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  14 KEAFTLFDTDGDGKISPSELGILMRSLGGNPTQAQLKSIIAeeKLTSPFDFNRFMELMSKHLKPEPFDR------QLRDA 87
Cdd:NF041410  30 KQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFS--DLDSDGDGSLSSDELAAAAPPPPPPPdqapstELADD 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 460411713  88 -FKVLDKDGTGFVVVSDLKHILTSIGEKLEPSEFdewIREVDAGSDGKIRYEDFIARM 144
Cdd:NF041410 108 lLSALDTDGDGSISSDELSAGLTSAGSSADSSQL---FSALDSDGDGSVSSDELAAAL 162
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 15-140 9.49e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 35.02  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460411713  15 EAFTLFDTDGDGKISPSELGILMRSL-----GGNPTQAQLKSIIAE--EKLTSPFDFNRFMELMSKHLKPEP-FDRQLRD 86
Cdd:cd15902    3 EVWMHFDADGNGYIEGKELDSFLRELlkalnGKDKTDDEVAEKKKEfmEKYDENEDGKIEIRELANILPTEEnFLLLFRR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 460411713  87 ------------AFKVLDKDGTGFVVVSDLKHILTSI----GEKLEPSEFDEWI----REVDAGSDGKIRYEDF 140
Cdd:cd15902   83 eqplissvefmkIWRKYDTDGSGFIEAKELKGFLKDLllknKKHVSPPKLDEYTklilKEFDANKDGKLELDEM 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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